Heikkinen S, Aitio H, Permi P, Folmer R, Lappalainen K, Kilpeläinen I
Institute of Biotechnology, University of Helsinki, FIN-00014, Finland.
J Magn Reson. 1999 Mar;137(1):243-6. doi: 10.1006/jmre.1998.1661.
A new method for the measurement of homonuclear 3J(HNHalpha) coupling constants in 15N-labeled small proteins is described. The method is based on a modified sensitivity enhanced HSQC experiment, where the 3J(HNHalpha) couplings are multiplied in the f1-dimension. The J-multiplication of homonuclear 3J(HNHalpha) couplings is based on simultaneous incrementation of 15N chemical shift and homonuclear coupling evolution periods. The time increment for the homonuclear coupling evolution period is chosen to be a suitable multiple (2N x t1) of the corresponding increment for 15N-shift evolution. This results in the splitting of the HSQC correlation in the f1-dimension by 2N x 3J(HNHalpha). Because the pulse sequence has good sensitivity and water suppression properties, it is particularly useful for natural abundance samples.
本文描述了一种用于测量15N标记的小蛋白质中同核3J(HNHα)耦合常数的新方法。该方法基于一种改进的灵敏度增强HSQC实验，其中3J(HNHα)耦合在f1维度上进行相乘。同核3J(HNHα)耦合的J相乘基于15N化学位移和同核耦合演化期的同时增加。同核耦合演化期的时间增量被选择为15N位移演化相应增量的合适倍数(2N×t1)。这导致HSQC相关峰在f1维度上被2N×3J(HNHα)分裂。由于该脉冲序列具有良好的灵敏度和水抑制特性，它对天然丰度样品特别有用。
